Research workbench
Crystal structure of cyma from klebsiella oxytoca
Analyse Crystal structure of cyma from klebsiella oxytoca in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D51
- Type
- protein
- Length
- 312 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyma
- UniProt
- Q48391
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 1% helix, 76% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyma | protein | 312 | 1% helix, 76% strand | Q48391 |
Ligands and binding sites
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 952 | 0.81 | 0.83 | 88 | empty |
| 2 | 148 | 0.61 | 0.84 | 38 | empty |
Compared structures
- 4D51 · Crystal structure of CymA from Klebsiella oxytoca · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q48391
- Elsewhere: RCSB PDB 4D51 · PDBe 4D51 · UniProt Q48391
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